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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Hyperphosphorylation tunes TDP-43 solubility.

Garrett M Ginell^1,2, Alex S Holehouse^1,2

¹Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.

The EMBO Journal

|March 21, 2022

Summary

Post-translational modifications alter intrinsically disordered regions (IDRs), affecting protein behavior. This study examines hyperphosphorylation

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Chemical Triphosphorylation of Oligonucleotides

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Chemical Triphosphorylation of Oligonucleotides

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Published on: June 2, 2022

Area of Science:

Biochemistry
Molecular Biology
Neuroscience

Background:

Intrinsically disordered regions (IDRs) lack stable structures but are crucial for cellular functions.
Post-translational modifications (PTMs) dynamically alter IDR properties.
TDP-43, a key IDR, is implicated in neurodegenerative diseases like Amyotrophic Lateral Sclerosis (ALS).

Purpose of the Study:

To investigate the impact of hyperphosphorylation on the C-terminal domain of TDP-43.
To understand how PTMs modulate the conformational dynamics and molecular interactions of TDP-43.

Main Methods:

Utilized biochemical assays to study TDP-43 phosphorylation.
Employed biophysical techniques to analyze conformational changes.
Investigated protein-protein interactions involving modified TDP-43.

Main Results:

Hyperphosphorylation significantly alters the sequence chemistry of TDP-43's C-terminal IDR.
These modifications induce distinct conformational states.
Altered conformations affect TDP-43's binding partners and interactions.

Conclusions:

Hyperphosphorylation is a critical regulator of TDP-43 function.
Modulating TDP-43 PTMs offers potential therapeutic avenues for ALS.
Understanding IDR PTMs is vital for deciphering disease mechanisms.